Detail Information for IndEnz0001000423
IED ID IndEnz0001000423
Enzyme Type ID amylase000423
Protein Name Beta-amylase
EC 3.2.1.2
1,4-alpha-D-glucan maltohydrolase
Gene Name BMY1 BA1
Organism Medicago sativa (Alfalfa)
Taxonomic Lineage cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae rosids fabids Fabales Fabaceae Papilionoideae 50 kb inversion clade NPAAA clade Hologalegina IRL clade Trifolieae Medicago (medics) Medicago sativa (Alfalfa)
Enzyme Sequence MATSNKNMLLNYVPVYVMLPLGVINVNNVFEDPDGLKEQLVQLRAAGVDGVMIDVWWGIIEQKGPKEYDWSAYKSLFQLVQKCGLKLQAIMSFHQCGGNVGDVVNIPLPKWVLDIGESDPDIFYTNRSGIRNQEYLSIGVDNKPIFHGRTAIEIYSDYMKSFRENMSDLLKSEVIIDIEVGLGPAGELRYPSYPQNQGWQFPGIGEFQCYDKYLRESFKAAAAKAGHSEWELPDDAGTYNDVPESTEFFKTNGTYLTEKGKFFLTWYSNQLLNHGDQILDEANKAFLGCKVKLAIKVSGIHWWYKAPNHAAELTAGYYNLDDRDGYRPIAKIVSRHHAILNFTCLEMRDSEQSSDAHSSPQKLVQQVLSGGWRENIEVAGENALSRYDATAYNQIILNARPQGVNKDGPPKLRMYGVTYLRLSDDLMQQSNFDIFKKFVVKMHADQDYCSDPEKYNHGIPPLKRSGPKIPDDVLNEATKPIPPFPWDSETDMKVDG
Enzyme Length 496
Uniprot Accession Number O22585
Absorption
Active Site ACT_SITE 187; /note=Proton donor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10050; ACT_SITE 381; /note=Proton acceptor; /evidence=ECO:0000250|UniProtKB:P10538
Activity Regulation
Binding Site BINDING 54; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P10538; BINDING 94; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P10538; BINDING 102; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P10538; BINDING 296; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P10538; BINDING 301; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P10538; BINDING 343; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P10538; BINDING 421; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P10538
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains.; EC=3.2.1.2;
DNA Binding
EC Number 3.2.1.2
Enzyme Function
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (2); Binding site (7); Chain (1); Region (2)
Keywords Carbohydrate metabolism;Glycosidase;Hydrolase;Polysaccharide degradation
Interact With
Induction
Subcellular Location
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 56,140
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda